Q54JL7 (CNRN_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase cnrN
EC=3.1.3.67

Gene names

Name:	cnrN
ORF Names:	DDB_G0287969

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein phosphatase that negatively regulates PI3K-dependent pathways. Regulates cAMP signal transduction to control territory size. During development, a lawn of Dictyostelium cells breaks up into territories where cells aggregate in dendritic streams to form groups of 20'000 cells. Ref.2
Catalytic activity	Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate. Ref.2
Cofactor	Magnesium By similarity.
Developmental stage	Level is low in vegetative cells, increases after starvation, peaks between 5 and 10 hours, and then decreases. Aggregation territories and streams form after 5 to 8 hours of starvation. This pattern of accumulation indicates that cnrN mRNA is present when aggregation territories and streams are forming. Ref.2
Disruption phenotype	Cells lacking cnrN form abnormally small groups, which can be rescued by the expression of exogenous cnrN. They also overaccumulate cAMP during development and form abnormally small fruiting bodies. Five seconds after cAMP stimulation, a prolonged and higher peak of phosphatidylinositol (3,4,5)-trisphosphate is shown compared to wild type cells. Ref.2
Sequence similarities	Contains 1 C2 tensin-type domain. Contains 1 phosphatase tensin-type domain.

Ontologies

Keywords
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aggregation involved in sorocarp development Inferred from mutant phenotype Ref.2. Source: dictyBase negative regulation of actin filament depolymerization Inferred from mutant phenotype Ref.2. Source: dictyBase negative regulation of cAMP biosynthetic process Inferred from mutant phenotype Ref.2. Source: dictyBase regulation of phosphatidylinositol 3-kinase cascade Inferred from mutant phenotype Ref.2. Source: dictyBase
Molecular function	phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine phosphatase activity Inferred from electronic annotation. Source: InterPro protein tyrosine/serine/threonine phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 639	639	Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase cnrN		PRO_0000363860
Regions
	Domain	20 – 190	171	Phosphatase tensin-type
	Domain	195 – 350	156	C2 tensin-type
	Compositional bias	251 – 266	16	Poly-Asn
	Compositional bias	267 – 270	4	Poly-Gln
	Compositional bias	393 – 396	4	Poly-Asn
	Compositional bias	407 – 419	13	Poly-Thr
	Compositional bias	420 – 506	87	Ser-rich
	Compositional bias	513 – 547	35	Poly-Asn
Sites
	Active site	129	1	Phosphocysteine intermediate Potential

Sequences

	Sequence		Length	Mass (Da)
	Q54JL7 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: CF7DCEF658057929	FASTA	639	71,714
	10 20 30 40 50 60 MNQVFFSKIR SLVSADRHRF KSKEMDLDLD LSYITDNILA MGFPGTGLEA SWRNSIDDVC 70 80 90 100 110 120 ELLKQKHHGK YMIWNLSERV YDYSKLNNQI LEFPFLDHHP PPLSLLFEIV NSLSNWLKAD 130 140 150 160 170 180 AENVAVVHCK GGKGRTGTII CCYLYYSCQF EIMDDAKNHF AEKRSKMKKG VTQPSQQRYI 190 200 210 220 230 240 NYFKEIVSGS HMVEEFVLTF RSIELGPLTK DQANSLSFEI FEHAKEPILN FASSSNSIQI 250 260 270 280 290 300 VPINNDNSES NNNNNNNNNN NNNNNNQQQQ LYKIIILIQK KVQNDVLIRV YRGDTGKGKG 310 320 330 340 350 360 KMKKQIFHLI FNIAFVNLDQ CLFGMNEFDH FKSSKKYDPN LQMECRFQNN CTGAPDHSFK 370 380 390 400 410 420 IWNIMALQYQ RTKSSLNNSI TDIKSINEIN STNNNNILAS SAPTPLTTTT TTTTTTTTTS 430 440 450 460 470 480 LPSSEHSTPQ ILISSSDANL DLKNCNINCD SSSGGGSNSS RNSNSNSRGG SSNSSSNRSS 490 500 510 520 530 540 TSSRSSITTD SIKPSCSSDS ICNNSSICNN SCNNNNNNNN NNNNNNNNNN NNNNNNNNNK 550 560 570 580 590 600 NSNNNNNESS SNSNDDSDSE ASIRKRKNTL WSSGSSIKLK PSPNLSRLSL FNGHRQSFTK 610 620 630 KINPNNNEEN VDQKTLPILK KETNDPSESD IKNVEIIQD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"A protein with similarity to PTEN regulates aggregation territory size by decreasing cyclic AMP pulse size during Dictyostelium discoideum development." Tang Y., Gomer R.H. Eukaryot. Cell 7:1758-1770(2008) [PubMed: 18676953] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000107 Genomic DNA. Translation: EAL63410.1.
RefSeq	XP_636914.1. XM_631822.1.
3D structure databases
HSSP	HSSP built from PDB template 1D5R based on UniProtKB P60484.
ProteinModelPortal	Q54JL7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0229881; DDB0229881; DDB_G0287969.
GeneID	8626389.
GenomeReviews	Gene locus cnrN in contig CM000154_GR.
KEGG	ddi:DDB_G0287969.
Organism-specific databases
dictyBase	DDB_G0287969. cnrN.
Phylogenomic databases
eggNOG	KOG2283.
GeneTree	EPrGT00050000000027.
InParanoid	Q54JL7.
PhylomeDB	Q54JL7.
Family and domain databases
InterPro	IPR000340. Dual-sp_phosphatase_cat-dom. IPR014019. Phosphatase_tensin-typ. IPR014020. Tensin_phosphatase_C2-dom. IPR016130. Tyr_Pase_AS. [Graphical view]
Pfam	PF00782. DSPc. 1 hit. PF10409. PTEN_C2. 1 hit. [Graphical view]
PROSITE	PS51182. C2_TENSIN. 1 hit. PS51181. PPASE_TENSIN. 1 hit. PS00383. TYR_PHOSPHATASE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CNRN_DICDI

Accession

Primary (citable) accession number: Q54JL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	May 24, 2005
Last modified:	September 21, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)